Stimulation of inositide degradation in clumping Stigmatella aurantiaca.

Numerous external signals which activate inositol phospholipid hydrolysis in eukaryotes are known; probably all of these signals are transduced by G proteins. So far, neither signal-transducing G protein nor receptor-regulated phospholipase C has been found in prokaryotes. However, a group of bacteria, the myxobacteria, displays cellular and tissue-like differentiation; therefore, it appeared that a search for the various activities involved in a signal-activated phosphatidylinositol cycle might be rewarding. Here, we report that in Stigmatella aurantiaca, under conditions which promote clumping, inositol phospholipid synthesis and degradation were stimulated with the resulting formation of inositol phosphate and inositol bisphosphate. The turnover was Ca2+ dependent and was increased by fluoride ions. Membrane preparations from these cells showed a phospholipase C activity which increased with the stage of incubation and which was stimulated by GTP gamma S, suggesting G protein dependency. To what extent this system in a prokaryotic cell shares properties of the phosphatidylinositol cycle in eukaryotes remains unexamined.